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2VGG

HUMAN ERYTHROCYTE PYRUVATE KINASE: R479H MUTANT

Replaces:  1LIY
Summary for 2VGG
Entry DOI10.2210/pdb2vgg/pdb
Related2VGB 2VGF
DescriptorPYRUVATE KINASE ISOZYMES R/L, 1,6-di-O-phosphono-beta-D-fructofuranose, 2-PHOSPHOGLYCOLIC ACID, ... (5 entities in total)
Functional Keywordsmetal-binding, phosphorylation, pyruvate kinase in the active r-state, kinase, pyruvate, magnesium, glycolysis, transferase, disease mutation
Biological sourceHOMO SAPIENS (HUMAN)
Total number of polymer chains4
Total formula weight230181.84
Authors
Valentini, G.,Chiarelli, L.R.,Fortin, R.,Dolzan, M.,Galizzi, A.,Abraham, D.J.,Wang, C.,Bianchi, P.,Zanella, A.,Mattevi, A. (deposition date: 2007-11-13, release date: 2007-11-20, Last modification date: 2024-02-07)
Primary citationValentini, G.,Chiarelli, L.R.,Fortin, R.,Dolzan, M.,Galizzi, A.,Abraham, D.J.,Wang, C.,Bianchi, P.,Zanella, A.,Mattevi, A.
Structure and Function of Human Erythrocyte Pyruvate Kinase. Molecular Basis of Nonspherocytic Hemolytic Anemia.
J.Biol.Chem., 277:23807-, 2002
Cited by
PubMed: 11960989
DOI: 10.1074/JBC.M202107200
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.74 Å)
Structure validation

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